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Role of the modulator protein in the interconversion of rabbit skeletal muscle protein phosphatase.

Abstract：

:The major active protein phosphatase present in a rabbit skeletal muscle extract is associated with the glycogen particle and migrates in sucrose density gradient centrifugation as a Mr = 70,000 protein and contains modulator activity. Addition of extra modulator protein causes a time- and concentration-dependent conversion of the enzyme to an inactive FA-ATP, Mg-dependent form. The intrinsic modulator in the active phosphatase is destroyed by limited proteolysis without an appreciable change in the phosphatase activity. The proteolyzed active enzyme has a lower molecular weight (Mr = 40,000) and it reassociates with the modulator producing a FA-ATP, Mg-dependent enzyme form (Mr = 60,000). The modulator protein is used stoichiometrically in the activation of the ATP, Mg-dependent phosphatase. This is in agreement with the presence of one unit of modulator activity per unit of native spontaneously active phosphatase.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Vandenheede JR,Yang SD,Merlevede W

doi

10.1016/s0006-291x(83)80015-1

subject

Has Abstract

pub_date

1983-09-30 00:00:00

pages

871-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)80015-1

journal_volume

115

pub_type

杂志文章

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